Cited by 127HIV Research and TreatmentProtein Structure and DynamicsHIV/AIDS drug development and treatment

The DOI matches its Crossref record; 77 of the 77 references it cites were found in a registry or an index.

On the Role of the SP1 Domain in HIV-1 Particle Assembly: a Molecular Switch?

Open access

Datta, Siddhartha A. K., Temeselew, Lakew G., Crist, Rachael M., Soheilian, Ferri, Kamata, Anne, Mirro, Jane, Harvin, Demetria, Nagashima, Kunio, Cachau, Raul E., Rein, Alan·2011·Journal of Virology

DOI 10.1128/jvi.00006-11PMC PMC3126284

Open this paper in CoChat — free account

Abstract

Expression of a retroviral protein, Gag, in mammalian cells is sufficient for assembly of immature virus-like particles (VLPs). VLP assembly is mediated largely by interactions between the capsid (CA) domains of Gag molecules but is facilitated by binding of the nucleocapsid (NC) domain to nucleic acid. We have investigated the role of SP1, a spacer between CA and NC in HIV-1 Gag, in VLP assembly. Mutational analysis showed that even subtle changes in the first 4 residues of SP1 destroy the ability of Gag to assemble correctly, frequently leading to formation of tubes or other misassembled structures rather than proper VLPs. We also studied the conformation of the CA-SP1 junction region in solution, using both molecular dynamics simulations and circular dichroism. Consonant with nuclear magnetic resonance (NMR) studies from other laboratories, we found that SP1 is nearly unstructured in aqueous solution but undergoes a concerted change to an α-helical conformation when the polarity of the environment is reduced by addition of dimethyl sulfoxide (DMSO), trifluoroethanol, or ethanol. Remarkably, such a coil-to-helix transition is also recapitulated in an aqueous medium at high peptide concentrations. The exquisite sensitivity of SP1 to mutational changes and its ability to undergo a concentration-dependent structural transition raise the possibility that SP1 could act as a molecular switch to prime HIV-1 Gag for VLP assembly. We suggest that changes in the local environment of SP1 when Gag oligomerizes on nucleic acid might trigger this switch.

Integrity signals

Registry

Crossref · 10.1128/jvi.00006-11

Cites

77 of 77 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Estimation of Protein Secondary Structure from Circular Dichroism Spectra: Comparison of CONTIN, SELCON, and CDSSTR Methods with an Expanded Reference Set
Sreerama, N., & Woody, R. W. (2000) · Analytical Biochemistry · doi:10.1006/abio.2000.4880 · Cited by 3,046
Estimation of globular protein secondary structure from circular dichroism
Provencher, S. W., & Gloeckner, J. (1981) · Biochemistry · doi:10.1021/bi00504a006 · Cited by 2,165
The helical hydrophobic moment: a measure of the amphiphilicity of a helix
Eisenberg, D. S., Weiss, R. M., & Terwilliger, T. C. (1982) · Nature · doi:10.1038/299371a0 · Cited by 1,080
Trifluoroethanol and colleagues: cosolvents come of age. Recent studies with peptides and proteins
Buck, M. (1998) · Quarterly Reviews of Biophysics · doi:10.1017/s003358359800345x · Cited by 829
Measurement of protein by spectrophotometry at 205 nm
Scopes, R. K. (1974) · Analytical Biochemistry · doi:10.1016/0003-2697(74)90034-7 · Cited by 762
DICHROWEB: an interactive website for the analysis of protein secondary structure from circular dichroism spectra
Lobley, A., Whitmore, L., & Wallace, B. A. (2002) · Bioinform. · doi:10.1093/bioinformatics/18.1.211 · Cited by 741
Crystal Structure of Human Cyclophilin A Bound to the Amino-Terminal Domain of HIV-1 Capsid
Gamble, T. R., Vajdos, F. F., Yoo, S., Worthylake, D. K., Houseweart, M., Sundquist, W. I., & Hill, C. P. (1996) · Cell · doi:10.1016/s0092-8674(00)81823-1 · Cited by 706
Structure of the HIV-1 Nucleocapsid Protein Bound to the SL3 Ψ-RNA Recognition Element
De Guzman, R. N., Wu, Z. R., Stalling, C. C., Pappalardo, L., Borer, P. N., & Summers, M. F. (1998) · Science · doi:10.1126/science.279.5349.384 · Cited by 659
Isolierung und Kristallisation des G�rungsferments Zymohexase
Warburg, O. H., & Walter, C. A. (1942) · Die Naturwissenschaften · doi:10.1007/bf01488995 · Cited by 635
Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein
Gamble, T. R., Yoo, S., Vajdos, F. F., von Schwedler, U. K., Worthylake, D. K., Wang, H., McCutcheon, J. P., Sundquist, W. I., & Hill, C. P. (1997) · Science · doi:10.1126/science.278.5339.849 · Cited by 598
Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication
Compton, L. A., & Johnson, W. C. (1986) · Analytical Biochemistry · doi:10.1016/0003-2697(86)90241-1 · Cited by 577
Synthesis of a model protein of defined secondary and quaternary structure. Effect of chain length on the stabilization and formation of two-stranded alpha-helical coiled-coils.
Lau, S. Y. M., Taneja, A. K., & Hodges, R. S. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)90686-1 · Cited by 572
Synthesis, Assembly, and Processing of Viral Proteins
Swanstrom, R. I., & Wills, J. (1997) · Europe PMC (PubMed Central) · Cited by 518
Crystal structures of the trimeric human immunodeficiency virus type 1 matrix protein: implications for membrane association and assembly
Hill, C. P., Worthylake, D., Bancroft, D. P., Christensen, A. M., & Sundquist, W. I. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.7.3099 · Cited by 473
Trifluoroethanol-induced Stabilization of the α-Helical Structure of β-Lactoglobulin: Implication for Non-hierarchical Protein Folding
Shiraki, K., Nishikawa, K., & Goto, Y. (1995) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.0015 · Cited by 459
Structure of the Amino-Terminal Core Domain of the HIV-1 Capsid Protein
Gitti, R. K., Lee, B. M., Walker, J., Summers, M. F., Yoo, S., & Sundquist, W. I. (1996) · Science · doi:10.1126/science.273.5272.231 · Cited by 459
Viral Late Domains
Freed, E. O. (2002) · Journal of Virology · doi:10.1128/jvi.76.10.4679-4687.2002 · Cited by 423
Structure and assembly of immature HIV
Briggs, J. A. G., Riches, J. D., Glass, B., Bartonova, V., Zanetti, G., & Kräusslich, H.-G. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0903535106 · Cited by 368
Self-assembly in vitro of purified CA-NC proteins from Rous sarcoma virus and human immunodeficiency virus type 1
Campbell, S., & Vogt, V. M. (1995) · Journal of Virology · doi:10.1128/jvi.69.10.6487-6497.1995 · Cited by 350
NMR structure of the HIV-1 nucleocapsid protein bound to stem-loop SL2 of the psi-RNA packaging signal. Implications for genome recognition.
Amarasinghe, G., Guzman, R. D. D., Turner, R. B., Chancellor, K. J., Wu, Z.-R., & Summers, M. F. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3979 · Cited by 337
Sequential Steps in Human Immunodeficiency Virus Particle Maturation Revealed by Alterations of Individual Gag Polyprotein Cleavage Sites
Wiegers, K., Rutter, G., Kottler, H., Tessmer, U., Hohenberg, H., & Kräusslich, H.-G. (1998) · Journal of Virology · doi:10.1128/jvi.72.4.2846-2854.1998 · Cited by 336
Synthetic model proteins. Positional effects of interchain hydrophobic interactions on stability of two-stranded alpha-helical coiled-coils.
Zhou, N., Kay, C. M., & Hodges, R. S. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45932-7 · Cited by 335
Electron cryotomography of immature HIV‐1 virions reveals the structure of the CA and SP1 Gag shells
Wright, E. R., Schooler, J. B., Ding, H. J., Kieffer, C., Fillmore, C., Sundquist, W. I., & Jensen, G. J. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601664 · Cited by 325
RNA is a structural element in retrovirus particles
Muriaux, D. M., Mirro, J., Harvin, D., & Rein, A. R. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.091000398 · Cited by 315
Self-citation
In vitro assembly properties of human immunodeficiency virus type 1 Gag protein lacking the p6 domain
Campbell, S., & Rein, A. (1999) · Journal of Virology · doi:10.1128/jvi.73.3.2270-2279.1999 · Cited by 293
Self-citation
Efficient particle production by minimal gag constructs which retain the carboxy-terminal domain of human immunodeficiency virus type 1 capsid-p2 and a late assembly domain
Accola, M. A., Strack, B., & Göttlinger, H. G. (2000) · Journal of Virology · doi:10.1128/jvi.74.12.5395-5402.2000 · Cited by 288
Gag proteins of the highly replicative MN strain of human immunodeficiency virus type 1: posttranslational modifications, proteolytic processings, and complete amino acid sequences
Henderson, L. E., Bowers, M. A., Sowder, R. C., Serabyn, S. A., Johnson, D. G., Bess, J. W., Arthur, L. O., Bryant, D. K., & Fenselau, C. (1992) · Journal of Virology · doi:10.1128/jvi.66.4.1856-1865.1992 · Cited by 282
Three-dimensional structure of the human immunodeficiency virus type 1 matrix protein
Massiah, M. A., Starich, M. R., Paschall, C., Summers, M. F., Christensen, A. M., & Sundquist, W. I. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1719 · Cited by 271 · cited 1×
“MA (36, 49), the two domains within CA (28–30, 68), and NC”
Inactivation of the human immunodeficiency virus type 1 inhibitory elements allows Rev-independent expression of Gag and Gag/protease and particle formation
Schneider, R., Campbell, M., Nasioulas, G., Felber, B. K., & Pavlakis, G. N. (1997) · Journal of Virology · doi:10.1128/jvi.71.7.4892-4903.1997 · Cited by 254
Cryo-electron microscopy reveals ordered domains in the immature HIV-1 particle
Fuller, S. D., Wilk, T., Gowen, B. E., Kräusslich, H., & Vogt, V. M. (1997) · Current Biology · doi:10.1016/s0960-9822(06)00331-9 · Cited by 246
A conformational switch controlling HIV‐1 morphogenesis
Gross, I., Hohenberg, H., Wilk, T., Wiegers, K. J., Grättinger, M., Müller, B., Fuller, S., & Kräusslich, H. (2000) · The EMBO Journal · doi:10.1093/emboj/19.1.103 · Cited by 241
Structures of the HIV-1 capsid protein dimerization domain at 2.6 Å resolution
Worthylake, D. K., Wang, H., Yoo, S., Sundquist, W. I., & Hill, C. P. (1999) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998007689 · Cited by 235
Analysis of the Assembly Function of the Human Immunodeficiency Virus Type 1 Gag Protein Nucleocapsid Domain
Zhang, Y., Qian, H., Love, Z., & Barklis, E. (1998) · Journal of Virology · doi:10.1128/jvi.72.3.1782-1789.1998 · Cited by 225
A Set of Constructed Type Spectra for the Practical Estimation of Peptide Secondary Structure from Circular Dichroism
Reed, J., & Reed, T. A. (1997) · Analytical Biochemistry · doi:10.1006/abio.1997.2355 · Cited by 220
The spacer peptide between human immunodeficiency virus capsid and nucleocapsid proteins is essential for ordered assembly and viral infectivity
Kräusslich, H., Fäcke, M., Heuser, A. M., Konvalinka, J., & Zentgraf, H. (1995) · Journal of Virology · doi:10.1128/jvi.69.6.3407-3419.1995 · Cited by 215
Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag polyprotein
Tang, C., Ndassa, Y., & Summers, M. F. (2002) · Nature Structural Biology · doi:10.1038/nsb806 · Cited by 205
In Vitro Assembly Properties of Purified Bacterially Expressed Capsid Proteins of Human Immunodeficiency Virus
Gross, I., Hohenberg, H., & Kräusslich, H. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.t01-1-00592.x · Cited by 199
Modulation of HIV-like particle assembly in vitro by inositol phosphates
Campbell, S., Fisher, R. J., Towler, E. M., Fox, S. D., Issaq, H. J., Wolfe, T. L., Phillips, L. R., & Rein, A. R. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.191224698 · Cited by 199
Self-citation
A putative α-helical structure which overlaps the capsid-p2 boundary in the human immunodeficiency virus type 1 Gag precursor is crucial for viral particle assembly
Accola, M. A., Höglund, S., & Göttlinger, H. G. (1998) · Journal of Virology · doi:10.1128/jvi.72.3.2072-2078.1998 · Cited by 196
Supramolecular organization of immature and mature murine leukemia virus revealed by electron cryo-microscopy: Implications for retroviral assembly mechanisms
Yeager, M., Wilson-Kubalek, E. M., Weiner, S. G., Brown, P. O., & Rein, A. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.13.7299 · Cited by 189
Self-citation
Organization of Immature Human Immunodeficiency Virus Type 1
Wilk, T., Gross, I., Gowen, B. E., Rutten, T. L. M., de Haas, F., Welker, R., Kräusslich, H., Boulanger, P. A., & Fuller, S. D. (2001) · Journal of Virology · doi:10.1128/jvi.75.2.759-771.2001 · Cited by 179
Physical reasons for the unusual α-helix stabilization afforded by charged or neutral polar residues in alanine-rich peptides
Vila, J. A., Ripoll, D. R., & Scheraga, H. A. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.240455797 · Cited by 152
Conformation of the HIV-1 Gag Protein in Solution
Datta, S. A. K., Curtis, J. E., Ratcliff, W., Clark, P. K., Crist, R. M., Lebowitz, J., Krueger, S., & Rein, A. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.10.073 · Cited by 145
Self-citation
The Structure of Cucumber Mosaic Virus and Comparison to Cowpea Chlorotic Mottle Virus
Smith, T. J., Chase, E. S., Schmidt, T., & Perry, K. L. (2000) · Journal of Virology · doi:10.1128/jvi.74.16.7578-7586.2000 · Cited by 137
Interactions between HIV-1 Gag Molecules in Solution: An Inositol Phosphate-mediated Switch
Datta, S. A. K., Zhao, Z., Clark, P. K., Tarasov, S. G., Alexandratos, J. N., Campbell, S. J., Kvaratskhelia, M., Lebowitz, J., & Rein, A. R. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.10.072 · Cited by 132
Self-citation
The C-Terminal Half of the Human Immunodeficiency Virus Type 1 Gag Precursor Is Sufficient for Efficient Particle Assembly
Borsetti, A., Öhagen, Å., & Göttlinger, H. G. (1998) · Journal of Virology · doi:10.1128/jvi.72.11.9313-9317.1998 · Cited by 126
In Vitro Resistance to the Human Immunodeficiency Virus Type 1 Maturation Inhibitor PA-457 (Bevirimat)
Adamson, C. S., Ablan, S. D., Boeraș, I., Goila-Gaur, R., Soheilian, F., Nagashima, K., Li, F., Salzwedel, K., Sakalian, M., Wild, C. T., et al. (2006) · Journal of Virology · doi:10.1128/jvi.01369-06 · Cited by 124
Self-citation
Nucleic Acid-Independent Retrovirus Assembly Can Be Driven by Dimerization
Johnson, M. C., Scobie, H. M., Ma, Y. M., & Vogt, V. M. (2002) · Journal of Virology · doi:10.1128/jvi.76.22.11177-11185.2002 · Cited by 105
Characterization of Rous Sarcoma Virus Gag Particles Assembled In Vitro
Yu, F., Joshi, S., Ma, Y. M., Kingston, R., Simon, M., & Vogt, V. (2001) · Journal of Virology · doi:10.1128/jvi.75.6.2753-2764.2001 · Cited by 104
Characterization of a Putative α-Helix across the Capsid-SP1 Boundary That Is Critical for the Multimerization of Human Immunodeficiency Virus Type 1 Gag
Liang, C., Hu, J., Russell, R. S., Roldán, A., Kleiman, L., & Wainberg, M. A. (2002) · Journal of Virology · doi:10.1128/jvi.76.22.11729-11737.2002 · Cited by 103
Circular dichroism analyses of membrane proteins: An examination of differential light scattering and absorption flattening effects in large membrane vesicles and membrane sheets
Wallace, B. A., & Mao, D. (1984) · Analytical Biochemistry · doi:10.1016/0003-2697(84)90471-8 · Cited by 99
The Retroviral Capsid Domain Dictates Virion Size, Morphology, and Coassembly of Gag into Virus-Like Particles
Ako-adjei, D., Johnson, M. C., & Vogt, V. M. (2005) · Journal of Virology · doi:10.1128/jvi.79.21.13463-13472.2005 · Cited by 92
Assembly Properties of Human Immunodeficiency Virus Type 1 Gag-Leucine Zipper Chimeras: Implications for Retrovirus Assembly
Crist, R. M., Datta, S. A. K., Stephen, A. G., Soheilian, F., Mirro, J., Fisher, R. J., Nagashima, K., & Rein, A. R. (2008) · Journal of Virology · doi:10.1128/jvi.02031-08 · Cited by 90
Self-citation
Cryo-electron Microscopy Reveals Conserved and Divergent Features of Gag Packing in Immature Particles of Rous Sarcoma Virus and Human Immunodeficiency Virus
Briggs, J. A. G., Johnson, M. C., Simon, M. N., Fuller, S. D., & Vogt, V. M. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.10.025 · Cited by 89
Helical structure determined by NMR of the HIV‐1 (345–392)Gag sequence, surrounding p2: Implications for particle assembly and RNA packaging
Morellet, N., Druillennec, S., Lenoir, C., Bouaziz, S., & Roques, B. P. (2005) · Protein Science · doi:10.1110/ps.041087605 · Cited by 86
Dielectric Properties of Binary Solvent Mixtures of Dimethyl Sulfoxide with Water
Yang, L., Yang, X., Huang, K., Jia, G.-Z., & Shang, H. (2009) · International Journal of Molecular Sciences · doi:10.3390/ijms10031261 · Cited by 75
Rous Sarcoma Virus Gag Protein-Oligonucleotide Interaction Suggests a Critical Role for Protein Dimer Formation in Assembly
Ma, Y. M., & Vogt, V. M. (2002) · Journal of Virology · doi:10.1128/jvi.76.11.5452-5462.2002 · Cited by 74
Multiscale Computer Simulation of the Immature HIV-1 Virion
Ayton, G. S., & Voth, G. A. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2010.08.018 · Cited by 72
A Structurally Disordered Region at the C Terminus of Capsid Plays Essential Roles in Multimerization and Membrane Binding of the Gag Protein of Human Immunodeficiency Virus Type 1
Liang, C., Hu, J., Whitney, J. B., Kleiman, L., & Wainberg, M. A. (2003) · Journal of Virology · doi:10.1128/jvi.77.3.1772-1783.2003 · Cited by 72
Flexibility in the P2 domain of the HIV‐1 Gag polyprotein
Newman, J. L., Butcher, E. W., Patel, D. T., Mikhaylenko, Y., & Summers, M. F. (2004) · Protein Science · doi:10.1110/ps.04614804 · Cited by 71
Determinants of activity of the HIV-1 maturation inhibitor PA-457.
Li, F., Zoumplis, D., Matallana, C., Kilgore, N., Reddick, M., Yunus, A., Adamson, C. S., Salzwedel, K., Martin, D. E., Allaway, G., et al. (2006) · Virology · doi:10.1016/j.virol.2006.07.023 · Cited by 70
Nucleic Acid Binding-Induced Gag Dimerization in the Assembly of Rous Sarcoma Virus Particles In Vitro
Ma, Y. M., & Vogt, V. M. (2003) · Journal of Virology · doi:10.1128/jvi.78.1.52-60.2004 · Cited by 70
Synthesis, Assembly, and Processing of Viral Proteins -- Retroviruses
Jm, C., Sh, H., & He, V. (1997) · Cited by 64
Conserved and Variable Features of Gag Structure and Arrangement in Immature Retrovirus Particles
de Marco, A., Davey, N. E., Ulbrich, P., Phillips, J. M., Lux, V., Riches, J. D., Fuzik, T., Ruml, T., Kräusslich, H.-G., Vogt, V. M., et al. (2010) · Journal of Virology · doi:10.1128/jvi.01423-10 · Cited by 59
Genetic Determinants of Rous Sarcoma Virus Particle Size
Krishna, N. K., Campbell, S., Vogt, V., & Wills, J. (1998) · Journal of Virology · doi:10.1128/jvi.72.1.564-577.1998 · Cited by 57
Particle Size Determination.
Cadle, R. D. (1955) · Cited by 55
Mutation of the SP1 Sequence Impairs both Multimerization and Membrane-Binding Activities of Human Immunodeficiency Virus Type 1 Gag
Guo, X., Roldán, A., Hu, J., Wainberg, M. A., & Liang, C. (2005) · Journal of Virology · doi:10.1128/jvi.79.3.1803-1812.2005 · Cited by 53
Human Immunodeficiency Virus Type 1
Caliendo, A. M., & Kraft, C. S. (2016) · Springer eBooks · doi:10.1007/978-3-319-19674-9_45 · Cited by 51
Impact of human immunodeficiency virus Type 1 resistance to protease inhibitors on evolution of resistance to the maturation inhibitor Bevirimat (PA-457)
Adamson, C. S., Waki, K., Ablan, S. D., Salzwedel, K., & Freed, E. O. (2009) · Journal of Virology · doi:10.1128/jvi.02659-08 · Cited by 48
Preparation of Recombinant HIV-1 Gag Protein and Assembly of Virus-Like Particles In Vitro
Datta, S. A. K., & Rein, A. R. (2009) · Methods in molecular biology · doi:10.1007/978-1-59745-170-3_14 · Cited by 43
Self-citation
Mutations in the Spacer Peptide and Adjoining Sequences in Rous Sarcoma Virus Gag Lead to Tubular Budding
Keller, P. W., Johnson, M. C., & Vogt, V. M. (2008) · Journal of Virology · doi:10.1128/jvi.00213-08 · Cited by 40
Charged Assembly Helix Motif in Murine Leukemia Virus Capsid: an Important Region for Virus Assembly and Particle Size Determination
Cheslock, S. R., Poon, D. T. K., Fu, W., Rhodes, T. D., Henderson, L. E., Nagashima, K., McGrath, C. F., & Hu, W.-S. (2003) · Journal of Virology · doi:10.1128/jvi.77.12.7058-7066.2003 · Cited by 39
Self-citation
Effects of Blocking Individual Maturation Cleavages in Murine Leukemia Virus Gag
Oshima, M., Muriaux, D. M., Mirro, J., Nagashima, K., Dryden, K. A., Yeager, M. J., & Rein, A. R. (2004) · Journal of Virology · doi:10.1128/jvi.78.3.1411-1420.2004 · Cited by 37
Self-citation
Kinetic and conformational properties of a novel T‐cell antigen receptor transmembrane peptide in model membranes
Amon, M. A., Ali, M., Bender, V., Hall, K. N., Aguilar, M., Aldrich-Wright, J. R., & Manolios, N. (2008) · Journal of Peptide Science · doi:10.1002/psc.987 · Cited by 26
Important Role for the CA-NC Spacer Region in the Assembly of Bovine Immunodeficiency Virus Gag Protein
Guo, X., Hu, J., Whitney, J., Russell, R., & Liang, C. (2004) · Journal of Virology · doi:10.1128/jvi.78.2.551-560.2004 · Cited by 22
Conformational changes of the N-terminal part of Mason-Pfizer monkey virus p12 protein during multimerization
Knejzlı́k, Z., Ulbrich, P., Strohalm, M., Laštůvková, H., Kodı́ček, M., Sakalian, M., & Ruml, T. (2009) · Virology · doi:10.1016/j.virol.2009.07.014 · Cited by 5
HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 MATRIX PROTEIN
Massiah, M. A., Starich, M. R., Paschall, C. M., Christensen, A. M., Sundquist, W. I., & Summers, M. F. (1995) · Worldwide Protein Data Bank · doi:10.2210/pdb2hmx/pdb · Cited by 2

Research works printed but not linked: 2

CreightonT. E. 1993. Proteins, 2nd ed. W. H. Freeman and Co., New York, NY.
WarburgO. ChristianW.. 1942. Isolierung und Kristallisation des Garungsferments Enolase. Biochem. Z. 310:384–421.

Sorted by citations

HIV-1 assembly, budding, and maturation
Sundquist, W. I., & Krausslich, H.-G. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006924 · Cited by 814
An atomic model of HIV-1 capsid-SP1 reveals structures regulating assembly and maturation
Schur, F. K. M., Obr, M., Hagen, W. J. H., Wan, W., Jakobi, A. J., Kirkpatrick, J. M., Sachse, C., Kräusslich, H., & Briggs, J. A. G. (2016) · Science · doi:10.1126/science.aaf9620 · Cited by 423
HIV Gag polyprotein: processing and early viral particle assembly
Bell, N. M., & Lever, A. M. L. (2013) · Trends in Microbiology · doi:10.1016/j.tim.2012.11.006 · Cited by 222
Retroviral proteases and their roles in virion maturation
Konvalinka, J., Kräusslich, H.-G., & Müller, B. (2015) · Virology · doi:10.1016/j.virol.2015.03.021 · Cited by 148
Crystal structure of an HIV assembly and maturation switch
Wagner, J. M., Zadrozny, K. K., Chrustowicz, J., Purdy, M. D., Yeager, M. J., Ganser‐Pornillos, B. K., & Pornillos, O. (2016) · eLife · doi:10.7554/elife.17063 · Cited by 136

See all 127

Authors: Datta, S. A. K., Temeselew, L. G., Crist, R. M., Soheilian, F., Kamata, A., Mirro, J., Harvin, D., Nagashima, K., Cachau, R. E., & Rein, A.
Affiliations: National Cancer Institute (US)
Science Applications International Corporation (United States) (US)
Information Systems Program, SAIC-Frederick, Inc., Frederick, Maryland 21702-1201
Corresponding author: Datta, Siddhartha A. K.
Rein, Alan
ORCID: Datta, Siddhartha A. K.
Crist, Rachael M.
Nagashima, Kunio
Rein, Alan
Venue: Journal of Virology
Publisher: American Society for Microbiology
Published: 2011-05
Volume: 85
Issue: 9
Pages: 4111-4121
ISSN: 0022-538X (ISSN-L)
1098-5514
DOI: 10.1128/jvi.00006-11
PMC: PMC3126284
OpenAlex: W2115382947
Cited by: 127
References: 77
Citations by year: 2026: 5 · 2025: 1 · 2024: 4 · 2023: 3 · 2022: 4 · 2021: 6 · 2020: 10 · 2019: 6 · 2018: 8 · 2017: 13 · 2016: 12 · 2015: 19 · 2014: 9 · 2013: 9 · 2012: 15
FWCI: 4.56
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Journal of Virology (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
U.S. Public Health Service (26120080001E)
Topics: Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Health Sciences › Medicine › Infectious Diseases › HIV/AIDS drug development and treatment
Keywords: HIV-1 Gag, virus-like particle assembly, capsid protein, nucleocapsid protein, molecular switches, helix-coil transition, protein conformational change, retroviral assembly
MeSH terms: Animals, Circular Dichroism, DNA Mutational Analysis, Protein Conformation, HIV-1, Virus Assembly, Virosomes, gag Gene Products, Human Immunodeficiency Virus, Molecular Dynamics Simulation

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

On the Role of the SP1 Domain in HIV-1 Particle Assembly: a Molecular Switch?

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks